Analytical Data
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Gene name
PHYH
- Application
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Alternative Names
PHYH；PAHX；Phytanoyl-CoA dioxygenase. peroxisomal
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O14832
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Expression Region
1-338aa
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AA Sequence
SGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
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Molecular Weight
62.4kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of PHYH (phytanoyl-CoA 2-hydroxylase) recombinant proteins has gained significant attention due to their crucial role in the metabolism of fatty acids, particularly in the degradation of phytanic acid, a branched-chain fatty acid derived from dietary sources. Mutations in the PHYH gene can lead to a rare genetic disorder known as Refsum disease, characterized by the accumulation of phytanic acid in tissues, resulting in various neurological and visual impairments. Research on recombinant PHYH proteins aims to enhance our understanding of the enzyme's structure, function, and catalytic mechanisms. By producing these proteins in a lab setting, scientists can investigate the enzyme's activity, explore its binding affinity to phytanic acid and related substrates, and identify potential therapeutic targets. Furthermore, recombinant PHYH proteins serve as valuable tools for studying enzyme regulation and understanding the broader implications of fatty acid metabolism in health and disease. Through the development of high-yield expression systems and purification techniques, current studies seek to elucidate the biochemical pathways involved in lipid metabolism and to assess the potential of gene therapy or enzyme replacement strategies for treating Refsum disease and related conditions. Overall, the exploration of PHYH recombinant proteins is a promising avenue for advancing genetic understanding, developing novel therapies, and improving the quality of life for individuals affected by metabolic disorders associated with fatty acid accumulation.
